Analytical Data
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Gene name
RPL22
- Application
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Alternative Names
RPL22;Large ribosomal subunit Protein eL22
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P35268
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Expression Region
1-128aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAPVKKL VVKGGKKKKQ VLKFTLDCTH PVEDGIMDAA NFEQFLQERI KVNGKAGNLG GGVVTIERSK SKITVTSEVP FSKRYLKYLT KKYLKKNNLR DWLRVVANSK ESYELRYFQI NQDEEEEEDE D
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Molecular Weight
17 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
RPL22, a ribosomal protein located in the 60S subunit of the ribosome, plays a crucial role in protein synthesis within eukaryotic cells. Recent studies have indicated that RPL22 is involved not only in ribosome biogenesis but also in various cellular processes, including stress responses and cell proliferation. Importantly, aberrations in RPL22 expression have been linked to several diseases, including cancer, where its downregulation can lead to disrupted protein synthesis and altered cell signaling pathways. Researchers have been exploring RPL22 as a potential biomarker for tumor progression and a target for therapeutic intervention. The recombinant expression of RPL22 provides a valuable tool for investigating its functional roles and interactions in ribosome assembly and cellular functions. By producing RPL22 as a recombinant protein, scientists can conduct detailed studies on its structure, binding properties, and regulatory mechanisms. This research could illuminate the significance of RPL22 in both normal physiological processes and disease states, offering insights into novel therapeutic strategies aimed at modulating its function or compensating for its loss in disease contexts. Overall, the investigation of RPL22 and its recombinant form holds promise for advancing our understanding of fundamental biological processes and their implications in human health and disease.
